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Isolation and Properties of Alginate Lyase from the Mid-Gut Gland of Wreath Shell Turbo cornutus
Authors:Tsuyoshi Muramatsu  Shigenori Hirose  Makiko Katayose
Affiliation:Laboratory of Fisheries Chemistry, Faculty of Fisheries, Nagasaki University, Nagasaki
Abstract:Alginate lyase [EC 4.2.2.3] has been purified from mid-gut gland of wreath shell. The enzyme was homogeneous as judged by SDS-polyacrylamide gel electrophoresis. A molecular weight of 32,000 was estimated by SDS-polyacrylamide gel electrophoresis. Absorption spectra of the reaction products indicated that the enzyme had lyase activity. The enzyme was most active at a pH range of about 8.8 to 9.2 and most stable at pH 5 to 6. Phosphate showed strong stabilizing and enhancing effects on the enzyme activity. Divalent cations behaved differently toward alginic acid and propylene glycol alginate, suggesting requirements for free carboxyl groups and a single glycosidic chain in the enzyme action.
Keywords:medium-chain triglyceride  white adipose tissue  hormone-sensitive lipase  cyclic adenosine monophosphate  protein kinase A
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